메뉴 건너뛰기




Volumn 4, Issue 2, 1997, Pages 105-117

Consensus chemistry and β-turn conformation of the active core of the insect kinin neuropeptide family

Author keywords

cis proline; molecular dynamics; nuclear magnetic resonance; receptor binding; signal transduction

Indexed keywords

ANIMALIA; GRYLLIDAE; INSECTA;

EID: 0030983698     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(97)90254-4     Document Type: Article
Times cited : (55)

References (37)
  • 1
    • 0017735536 scopus 로고
    • Endogenous opioid peptides: Multiple agonists and receptors
    • Lord, J.A.H, Waterfield, A.A., Hughes, J. & Kosterlitz, H.W. (1977). Endogenous opioid peptides: multiple agonists and receptors. Nature 267, 495-499.
    • (1977) Nature , vol.267 , pp. 495-499
    • Lord, J.A.H.1    Waterfield, A.A.2    Hughes, J.3    Kosterlitz, H.W.4
  • 2
    • 0022856128 scopus 로고
    • Characterization of a neurokinin B receptor site in rat brain using a highly selective radioligand
    • Laufer, R., Gilon, C., Chorev, M. & Selinger, Z. (1986). Characterization of a neurokinin B receptor site in rat brain using a highly selective radioligand. J. Biol. Chem. 261, 10257-10263.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10257-10263
    • Laufer, R.1    Gilon, C.2    Chorev, M.3    Selinger, Z.4
  • 3
    • 0029132934 scopus 로고
    • Molecular organization of receptors: Efficacy, agonists, and antagonists
    • Hruby, V.J., Yamamura, H.I. & Porreca, F. (1995). Molecular organization of receptors: efficacy, agonists, and antagonists. Ann. N.Y. Acad. Sci. 757, 7-22.
    • (1995) Ann. N.Y. Acad. Sci. , vol.757 , pp. 7-22
    • Hruby, V.J.1    Yamamura, H.I.2    Porreca, F.3
  • 4
    • 0025336463 scopus 로고
    • Emerging approaches in the molecular design of receptor-selective peptide ligands: Conformational, topographical and dynamics considerations
    • Hruby, V.J., Al-Obeidi, F. & Kazmierski, W. (1990). Emerging approaches in the molecular design of receptor-selective peptide ligands: conformational, topographical and dynamics considerations. Biochem. J. 268, 249-262.
    • (1990) Biochem. J. , vol.268 , pp. 249-262
    • Hruby, V.J.1    Al-Obeidi, F.2    Kazmierski, W.3
  • 6
    • 0000904127 scopus 로고
    • Myotropic insect neuropeptide families from the cockroach Leucophaea maderaea: Structure-activity relationships
    • (Menn, J.J., Kelly, T.J. & Masler, E.P., eds) American Chemical Society, Washington DC, USA
    • Nachman, R.J. & Holman, G.M. (1991). Myotropic insect neuropeptide families from the cockroach Leucophaea maderaea: structure-activity relationships. In Insect Neuropeptides: Chemistry, Biology and Action. (Menn, J.J., Kelly, T.J. & Masler, E.P., eds) pp. 194-214, American Chemical Society, Washington DC, USA.
    • (1991) Insect Neuropeptides: Chemistry, Biology and Action. , pp. 194-214
    • Nachman, R.J.1    Holman, G.M.2
  • 7
    • 0026544088 scopus 로고
    • Locustakinin, a novel myotropic peptide from Locusta migratoria, isolation, primary structure and synthesis
    • Schoofs, L, Holman, G.M., Proost, P., Van Damme, J., Hayes, T.K. & DeLoof, A. (1992). Locustakinin, a novel myotropic peptide from Locusta migratoria, isolation, primary structure and synthesis. Regul. Pept. 37, 49-57.
    • (1992) Regul. Pept. , vol.37 , pp. 49-57
    • Schoofs, L.1    Holman, G.M.2    Proost, P.3    Van Damme, J.4    Hayes, T.K.5    DeLoof, A.6
  • 8
    • 0028085358 scopus 로고
    • Culekinin depolarizing peptide: A mosquito leucokinin-like peptide that influences insect Malpighian tubule ion transport
    • Hayes, T.K., et al., & Beyenbach, K.M. (1994). Culekinin depolarizing peptide: a mosquito leucokinin-like peptide that influences insect Malpighian tubule ion transport. Regul. Pept. 52, 235-248.
    • (1994) Regul. Pept. , vol.52 , pp. 235-248
    • Hayes, T.K.1    Beyenbach, K.M.2
  • 9
    • 0027959014 scopus 로고
    • Isolation and identification of three leucokinins from the mosquito Aedes aegypti
    • Veenslra, J.A. (1994). Isolation and identification of three leucokinins from the mosquito Aedes aegypti. Biochem. Biophys. Res. Commun. 202, 715-719.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 715-719
    • Veenslra, J.A.1
  • 10
    • 0000266416 scopus 로고
    • The diuretic activity of a series of cephalomyotropic neuropeptides, the achetakinins, on isolated Malpighian tubules of the house cricket, Acheta domesticus
    • Coast, G.M., Holman, G.M. & Nachman, R.J. (1990). The diuretic activity of a series of cephalomyotropic neuropeptides, the achetakinins, on isolated Malpighian tubules of the house cricket, Acheta domesticus. J. Insect Physiol. 36, 481-488.
    • (1990) J. Insect Physiol. , vol.36 , pp. 481-488
    • Coast, G.M.1    Holman, G.M.2    Nachman, R.J.3
  • 11
    • 0024314883 scopus 로고
    • Leucokinins, a new family of ion transport stimulators and inhibitors in insect Malpighian tubules
    • Hayes, T.K., et al., & Beyenbach, K.W. (1989). Leucokinins, a new family of ion transport stimulators and inhibitors in insect Malpighian tubules. Life Sci. 44, 1259-1266.
    • (1989) Life Sci. , vol.44 , pp. 1259-1266
    • Hayes, T.K.1    Beyenbach, K.W.2
  • 12
    • 0017709445 scopus 로고
    • β-Turns in proteins
    • Chou, P.Y. & Fasman, S.D. (1977). β-Turns in proteins. J. Mol. Biol. 115, 135-176.
    • (1977) J. Mol. Biol. , vol.115 , pp. 135-176
    • Chou, P.Y.1    Fasman, S.D.2
  • 13
    • 0028566270 scopus 로고
    • A revised set of potentials for β-turn formation in proteins
    • Hutchinson, E.G. & Thornton, J.M. (1994). A revised set of potentials for β-turn formation in proteins. Protein Sci. 3, 2207-2216.
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 14
    • 0024278597 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution
    • Dyson, H.J., Rance, M., Houghten, R.A., Lerner, R.A. & Wright, P.E. (1988). Folding of immunogenic peptide fragments of proteins in water solution. J. Mol. Biol. 201, 161-200.
    • (1988) J. Mol. Biol. , vol.201 , pp. 161-200
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Lerner, R.A.4    Wright, P.E.5
  • 15
    • 0028068045 scopus 로고
    • Stabilization of a type VI turn in a family of linear peptides in water solution
    • Yao, J., Feher, V.A., Espejo, B.F., Reymond, M.T., Wright, P.E. & Dyson, H.J. (1994). Stabilization of a type VI turn in a family of linear peptides in water solution. J. Mol. Biol. 243, 736-753.
    • (1994) J. Mol. Biol. , vol.243 , pp. 736-753
    • Yao, J.1    Feher, V.A.2    Espejo, B.F.3    Reymond, M.T.4    Wright, P.E.5    Dyson, H.J.6
  • 16
    • 0027937869 scopus 로고
    • Three-dimensional structure of a type VI turn in a linear peptide in water solution
    • Yao, J., Dyson, H.J. & Wright, P.E. (1994). Three-dimensional structure of a type VI turn in a linear peptide in water solution. J. Mol. Biol. 243, 754-766.
    • (1994) J. Mol. Biol. , vol.243 , pp. 754-766
    • Yao, J.1    Dyson, H.J.2    Wright, P.E.3
  • 17
    • 84985715908 scopus 로고
    • NMR studies of the rates of proline cis-trans isomerization in oligopeptides
    • Grathwohl, C. & Wuthrich, K. (1981). NMR studies of the rates of proline cis-trans isomerization in oligopeptides. Biopolymers 20, 2623-2633.
    • (1981) Biopolymers , vol.20 , pp. 2623-2633
    • Grathwohl, C.1    Wuthrich, K.2
  • 19
    • 0027265411 scopus 로고
    • Active conformation of the pyrokinin/PBAN neuropeptide family for pheromone biosynthesis in the silkmoth Bombyx mori
    • Nachman, R.J., Kunlyoshi, H., Roberts, V.A., Holman, G.M. & Suzuki, A. (1993). Active conformation of the pyrokinin/PBAN neuropeptide family for pheromone biosynthesis in the silkmoth Bombyx mori. Biochem. Biophys. Res. Commun. 193, 661-666.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 661-666
    • Nachman, R.J.1    Kunlyoshi, H.2    Roberts, V.A.3    Holman, G.M.4    Suzuki, A.5
  • 20
    • 0022533517 scopus 로고
    • Active fragments and analogs of the insect neuropeptide leucopyrokinin: Structure-function studies
    • Nachman, R.J., Holman, G.M. & Cook, B.J. (1986). Active fragments and analogs of the insect neuropeptide leucopyrokinin: structure-function studies. Biochem. Biophys. Res. Commun. 137, 936-942.
    • (1986) Biochem. Biophys. Res. Commun. , vol.137 , pp. 936-942
    • Nachman, R.J.1    Holman, G.M.2    Cook, B.J.3
  • 23
    • 49149137679 scopus 로고
    • The tachykinin peptide family
    • Erspamer, V. (1981). The tachykinin peptide family. Trends in Neurosci. 4, 267-269.
    • (1981) Trends in Neurosci. , vol.4 , pp. 267-269
    • Erspamer, V.1
  • 24
    • 0001394003 scopus 로고
    • Active transport of water by the Malpighian tubules of the stick insect, Dixippus morosus (Orthoptera, Phasmidae)
    • Ramsay, J.A. (1954). Active transport of water by the Malpighian tubules of the stick insect, Dixippus morosus (Orthoptera, Phasmidae). J. Exp. Biol. 31, 104-113.
    • (1954) J. Exp. Biol. , vol.31 , pp. 104-113
    • Ramsay, J.A.1
  • 25
    • 0028152206 scopus 로고
    • The effects of Acheta diuretic peptide on isolated Malpighian tubules from the house cricket, Acheta domesticus
    • Coast, G.M. & Kay, I. (1994). The effects of Acheta diuretic peptide on isolated Malpighian tubules from the house cricket, Acheta domesticus. J. Exp. Biol. 187, 225-243.
    • (1994) J. Exp. Biol. , vol.187 , pp. 225-243
    • Coast, G.M.1    Kay, I.2
  • 26
    • 0002530334 scopus 로고
    • Insect myotropic peptides: Isolation, structural characterization and biological properties
    • (Menn, J.J., Kelly, T.J. & Masler, E.P., eds) American Chemical Society, Washington DC, USA
    • Holman, G.M., Nachman, R.J., Wright, M.S., Schoofs, L & DeLoof, A. (1991). Insect myotropic peptides: isolation, structural characterization and biological properties. In Insect Neuropeptides: Chemistry, Biology and Action. (Menn, J.J., Kelly, T.J. & Masler, E.P., eds) pp. 40-50, American Chemical Society, Washington DC, USA.
    • (1991) Insect Neuropeptides: Chemistry, Biology and Action , pp. 40-50
    • Holman, G.M.1    Nachman, R.J.2    Wright, M.S.3    Schoofs, L.4    DeLoof, A.5
  • 27
    • 0028998772 scopus 로고
    • Properties of achetakinin binding sites on Malpighian tubule membranes from the house cricket, Acheta domesticus
    • Chung, J.S., Wheeler, C.H., Goldsworthy, G.J. & Coast, G.M. (1995). Properties of achetakinin binding sites on Malpighian tubule membranes from the house cricket, Acheta domesticus. Peptides 16, 375-382.
    • (1995) Peptides , vol.16 , pp. 375-382
    • Chung, J.S.1    Wheeler, C.H.2    Goldsworthy, G.J.3    Coast, G.M.4
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0022996473 scopus 로고
    • Leucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin
    • Nachman, R.J, Holman, G.M., Haddon, W.F. & Ling, N. (1986). Leucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin. Science 234, 71-73.
    • (1986) Science , vol.234 , pp. 71-73
    • Nachman, R.J.1    Holman, G.M.2    Haddon, W.F.3    Ling, N.4
  • 31
    • 0000816329 scopus 로고
    • Compatibility of β- and γ-turn features with a peptide backbone modification: Synthesis and conformational analysis of a model cyclic pseudopentapeptide
    • Spatola, A.F., Anwer, M.K., Rockwell, A.L. & Gierasch, L.M. (1986). Compatibility of β- and γ-turn features with a peptide backbone modification: synthesis and conformational analysis of a model cyclic pseudopentapeptide. J. Amer. Chem. Soc. 108, 825-831.
    • (1986) J. Amer. Chem. Soc. , vol.108 , pp. 825-831
    • Spatola, A.F.1    Anwer, M.K.2    Rockwell, A.L.3    Gierasch, L.M.4
  • 33
  • 34
    • 0023769808 scopus 로고
    • Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system
    • Dauber-Osguthorpe, P., Roberts, V.A., Osguthorpe, D.J., Wolff, J., Genest, M. & Hagler, A.T. (1988). Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system. Proteins 4, 31-47.
    • (1988) Proteins , vol.4 , pp. 31-47
    • Dauber-Osguthorpe, P.1    Roberts, V.A.2    Osguthorpe, D.J.3    Wolff, J.4    Genest, M.5    Hagler, A.T.6
  • 36
    • 0021893184 scopus 로고
    • Molecular dynamics and minimum energy conformations of GnRH and analogs
    • Struthers, R.S., Rivier, J. & Hagler, A.T. (1985). Molecular dynamics and minimum energy conformations of GnRH and analogs. Ann. N.Y. Acad. Sci. 439, 81-96.
    • (1985) Ann. N.Y. Acad. Sci. , vol.439 , pp. 81-96
    • Struthers, R.S.1    Rivier, J.2    Hagler, A.T.3
  • 37
    • 0024700676 scopus 로고
    • The application visualization system: A computational environment for scientific visualization
    • Upson, C., et al., & van Dam, A. (1989). The application visualization system: a computational environment for scientific visualization. IEEE Comp. Graph. Appl. 9, 30-42.
    • (1989) IEEE Comp. Graph. Appl. , vol.9 , pp. 30-42
    • Upson, C.1    Van Dam, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.